the bifunctional enzyme of Cochlearia officinalis is not stereospecific, in contrast to the Solanaceae species, and catalyzes both tropinone reductase reactions, a tyrosine residue in the active site of Cochlearia officinalis TR is responsible for binding and orientation of tropinone, overview

the bifunctional enzyme of Cochlearia officinalis is not stereospecific, in contrast to the Solanaceae species, and catalyzes both tropinone reductase reactions, a tyrosine residue in the active site of Cochlearia officinalis TR is responsible for binding and orientation of tropinone, overview

689548

Cochlearia officinalis

?

-

-

-

-

additional information

the enzyme shows broad substrate specificity, several synthetic ketones are accepted as substrates, with higher affinity and faster enzymatic turnover than observed for tropinone, overview

the bifunctional enzyme of Cochlearia officinalis is not stereospecific, in contrast to the Solanaceae species, and catalyzes both tropinone reductase reactions, a tyrosine residue in the active site of Cochlearia officinalis TR is responsible for binding and orientation of tropinone, overview

the bifunctional enzyme of Cochlearia officinalis is not stereospecific, in contrast to the Solanaceae species, and catalyzes both tropinone reductase reactions, a tyrosine residue in the active site of Cochlearia officinalis TR is responsible for binding and orientation of tropinone, overview

689548

Cochlearia officinalis

?

-

-

-

-

additional information

the enzyme shows broad substrate specificity, several synthetic ketones are accepted as substrates, with higher affinity and faster enzymatic turnover than observed for tropinone, overview